Acetylglutamate kinase
| Acetylglutamate kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.2.8 | ||||||||
| CAS no. | 9027-58-1 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Acetylglutamate kinase (EC 2.7.2.8) is an enzyme that catalyzes the chemical reaction:
-N-Acetylglutamic_acid.svg.png)
The enzyme characterised from the bacterium, Escherichia coli and the green algae, Chlamydomonas reinhardti, converts N-acetyl-L-glutamic acid to N-acetyl-L-γ-glutamyl phosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP). The reaction is part of the biosynthesis of arginine.[1][2]
This enzyme is a transferase, specifically one transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor.[3]
Nomenclature
The systematic name of this enzyme class is ATP:N-acetyl-L-glutamate 5-phosphotransferase. Other names in common use include:[4]
- N-acetylglutamate 5-phosphotransferase,
- acetylglutamate phosphokinase,
- N-acetylglutamate phosphokinase,
- N-acetylglutamate kinase, and
- N-acetylglutamic 5-phosphotransferase.
Structural studies
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1GS5, PDB: 1GSJ, PDB: 1OH9, PDB: 1OHA, PDB: 1OHB, PDB: 2AP9, PDB: 2BTY, PDB: 2BUF, and PDB: 2RD5.
References
- ↑ Baich A, Vogel HJ (1962). "N-Acetyl-gamma-Ilutamokinase and N-acetylglutamic gamma-semialdehyde dehydrogenase: repressible enzymes of arginine synthesis in Escherichia coli". Biochem. Biophys. Res. Commun. 7 (6): 491–6. Bibcode:1962BBRC....7..491B. doi:10.1016/0006-291X(62)90342-X. PMID 13863980.
- ↑ Farago A, Denes G (1967). "Mechanism of arginine biosynthesis in Chlamydomonas reinhardti. II Purification and properties of N-acetylglutamate 5-phosphotransferase, the allosteric enzyme of the pathway". Biochim. Biophys. Acta. 136 (1): 6–18. doi:10.1016/0304-4165(67)90315-7. PMID 6040410.
- ↑ Vogel HJ, McLellan WL (1970). "[24b] N-acetyl-γ-glutamokinase (Escherichia coli)". N-Acetyl-gamma-glutamokinase (Escherichia coli). Methods Enzymol. Vol. 17A. pp. 251–255. doi:10.1016/0076-6879(71)17190-x. ISBN 978-0-12-181874-6.
- ↑ Enzyme 2.7.2.8 at KEGG Pathway Database.